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The protein encoded by EXOC4 is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Additionally we are shipping Exocyst Complex Component 4 Proteins (4) and many more products for this protein.
Showing 10 out of 32 products:
Mouse (Murine) Polyclonal EXOC4 Primary Antibody for IHC, WB - ABIN350317
Beausoleil, Villén, Gerber, Rush, Gygi: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. in Nature biotechnology 2006
Show all 5 references for ABIN350317
Chicken Monoclonal EXOC4 Primary Antibody for IF, IP - ABIN968092
Charron, Nakamura, Bacallao, Wandinger-Ness: Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells. in The Journal of cell biology 2000
Show all 4 references for ABIN968092
Human Polyclonal EXOC4 Primary Antibody for ICC, IF - ABIN4352426
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
Chicken Polyclonal EXOC4 Primary Antibody for WB - ABIN2786600
Pohl, Jentsch: Final stages of cytokinesis and midbody ring formation are controlled by BRUCE. in Cell 2008
Human Monoclonal EXOC4 Primary Antibody for ELISA, WB - ABIN528409
Imai, Yoshie, Haga-Tsujimura, Nashida, Shimomura: Exocyst subunits are involved in isoproterenol-induced amylase release from rat parotid acinar cells. in European journal of oral sciences 2012
Sec5 (show EXOC2 Antibodies), Sec6 (show EXOC3 Antibodies) and Sec8 act as a complex, each member dependent on the others for proper localization and function
No evidence that Sec8 is required for basal neurotransmission, though glutamate (show GRIN2A Antibodies) receptor trafficking was mildly disrupted in sec8 mutants.
Sec8 regulate Bcl-2 (show BCL2 Antibodies) and Mcl-1 (show MCL1 Antibodies) expressions but not Bcl-xl (show BCL2L1 Antibodies) in malignant peripheral nerve sheath tumor cells.
Sec8 regulates histone-modifying proteins ATF2 (show ATF2 Antibodies) and RNF20 (show RNF20 Antibodies).
Sec8 knockdown in HSC3 cells resulted in reduced expressions of PAK1 (show PAK1 Antibodies) and PAK2 (show PAK2 Antibodies) by upregulating Pirh2 (show RCHY1 Antibodies) and Siah1 (show SIAH1 Antibodies) expression, which inhibited the ERK (show EPHB2 Antibodies) or p38 MAPK (show MAPK14 Antibodies) signalling pathway and cytokeratin8 phosphorylation and cell migration.
knockdown of Sec8 enhances the binding of JIP4 (show SPAG9 Antibodies) to MAPK (show MAPK1 Antibodies) kinase 4, thereby decreasing the phosphorylation of MAPK (show MAPK1 Antibodies) kinase 4, JNK (show MAPK8 Antibodies), and p38 (show CRK Antibodies).
Exome sequencing revealed a likely pathogenic mutation in three novel candidate MKS (show MKS1 Antibodies) disease genes-C5orf42 (show C5ORF42 Antibodies), EVC2 (show EVC2 Antibodies) and SEC8 (also known as EXOC4), which encodes an exocyst protein with an established role in ciliogenesis
High Sec8 expression is associated with progression of oral squamous-cell carcinoma by secretion of matrix metalloproteinases.
EXOC4 is involved in insulin (show INS Antibodies)-stimulated glucose transport and may be a candidate for an association with type 2 diabetes.
The exocyst subunits Sec3 (show EXOC1 Antibodies) and Sec8 interact with the polarity protein IQGAP1 (show IQGAP1 Antibodies) and that this interaction is triggered by active Cdc42 (show CDC42 Antibodies) and RhoA (show RHOA Antibodies), which are essential for matrix degradation.
SAP102 (show DLG3 Antibodies) interacts with the PDZ (show INADL Antibodies)-binding domain of Sec8, a member of the exocyst complex. Interactions between the two proteins are involved in the delivery of N-methyl-D-aspartate receptors to the cell surface in heterologous cells and neurons.
the exocyst complex serves to selectively regulate the docking of insulin (show INS Antibodies)-containing vesicles at sites of release close to the plasma membrane
Sec8 controls the directional movement of AMPA (show GRIA3 Antibodies) receptors towards synapses through PDZ (show INADL Antibodies)-dependent interactions.
Insulin (show INS Antibodies) stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes.
Interaction of Discs large 1 (Dlg1 (show DLG4 Antibodies)) with the Sec8 exocyst component promotes membrane addition, whereas with myotubularin-related protein 2 (Mtmr2 (show MTMR2 Antibodies)), negatively regulates membrane formation.
The amount of pectinaceous mucilage and seed coat structure in sec8 and exo70A1 exocyst mutants, was characterized.
An allelic series of six independent T-DNA mutations reveal a role for SEC8 in male gametophyte function.
SEC8 copurifies in a high molecular mass fraction of 900 kD, interacts with SEC6 (show EXOC3 Antibodies), and functions as a subunit in a exocyst complex that plays important roles in morphogenesis.
The protein encoded by this gene is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and functions of exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. The complex is also essential for the biogenesis of epithelial cell surface polarity. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
, funnel cakes
, SEC8 protein
, exocyst complex component 4
, SEC8-like 1
, exocyst complex component Sec8
, augmenter of liver regeneration (ALR) pseudogene
, secretory protein SEC8